ID   RASH_RAT                Reviewed;         189 AA.
AC   P20171;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   28-JUN-2011, entry version 93.
DE   RecName: Full=GTPase HRas;
DE   AltName: Full=H-Ras-1;
DE   AltName: Full=Transforming protein p21;
DE   AltName: Full=c-H-ras;
DE   AltName: Full=p21ras;
DE   Contains:
DE     RecName: Full=GTPase HRas, N-terminally processed;
DE   Flags: Precursor;
GN   Name=Hras1; Synonyms=Hras;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87064453; PubMed=3023901;
RA   Ruta M., Wolford R., Dhar R., Defeo-Jones D., Ellis R.W.,
RA   Scolnick E.M.;
RT   "Nucleotide sequence of the two rat cellular rasH genes.";
RL   Mol. Cell. Biol. 6:1706-1710(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX   PubMed=3027702; DOI=10.1073/pnas.84.3.774;
RA   Damante G., Filetti S., Rapoport B.;
RT   "Nucleotide sequence and characterization of the 5' flanking region of
RT   the rat Ha-ras protooncogene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:774-778(1987).
RN   [3]
RP   ISOPRENYLATION AT CYS-186, CLEAVAGE, AND METHYLATION AT CYS-186.
RX   MEDLINE=88263004; PubMed=3290900; DOI=10.1073/pnas.85.13.4643;
RA   Clarke S., Vogel J.P., Deschenes R.J., Stock J.;
RT   "Posttranslational modification of the Ha-ras oncogene protein:
RT   evidence for a third class of protein carboxyl methyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988).
RN   [4]
RP   INTERACTION WITH PLCE1, AND MUTAGENESIS OF ASN-26; THR-35; GLU-37;
RP   ASP-38; TYR-40; GLN-61 AND CYS-186.
RX   MEDLINE=21099252; PubMed=11179219; DOI=10.1093/emboj/20.4.743;
RA   Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.;
RT   "Phospholipase C(epsilon): a novel Ras effector.";
RL   EMBO J. 20:743-754(2001).
RN   [5]
RP   IDENTIFICATION IN A COMPLEX WITH BRAF; MAP2K1; MAPK3 AND RGS14, AND
RP   INTERACTION WITH RGS14.
RX   PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA   Willard F.S., Willard M.D., Kimple A.J., Soundararajan M.,
RA   Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J.,
RA   Zylka M.J., Snider W.D., Siderovski D.P.;
RT   "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT   effector.";
RL   PLoS ONE 4:E4884-E4884(2009).
RN   [6]
RP   INTERACTION WITH RGS14, AND SUBCELLULAR LOCATION.
RX   PubMed=19878719; DOI=10.1016/j.cellsig.2009.10.005;
RA   Shu F.J., Ramineni S., Hepler J.R.;
RT   "RGS14 is a multifunctional scaffold that integrates G protein and
RT   Ras/Raf MAPkinase signalling pathways.";
RL   Cell. Signal. 22:366-376(2010).
CC   -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity.
CC   -!- ENZYME REGULATION: Alternate between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine
CC       nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC       activating protein (GAP).
CC   -!- SUBUNIT: Forms a signaling complex with RASGRP1 and DGKZ. In its
CC       GTP-bound form interacts with PLCE1. Interacts with TBC1D10C.
CC       Interacts with RGL3 and RASSF5. Interacts with HSPD1. Interacts
CC       with PDE6D. Interacts with IKZF3 (By similarity). Found in a
CC       complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14.
CC       Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cell membrane; Lipid-anchor;
CC       Cytoplasmic side (By similarity). Golgi apparatus membrane; Lipid-
CC       anchor (By similarity). Note=Shuttles between the plasma membrane
CC       and the Golgi apparatus (By similarity). The active GTP-bound form
CC       is localized most strongly to membranes than the inactive GDP-
CC       bound form.
CC   -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous
CC       cycle of de- and re-palmitoylation regulates rapid exchange
CC       between plasma membrane and Golgi (By similarity).
CC   -!- PTM: S-nitrosylated; critical for redox regulation. Important for
CC       stimulating guanine nucleotide exchange. No structural
CC       perturbation on nitrosylation.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR   EMBL; M13011; AAA42009.1; -; Genomic_DNA.
DR   EMBL; M15188; AAA42008.1; -; Genomic_DNA.
DR   IPI; IPI00196529; -.
DR   PIR; A25229; A25229.
DR   UniGene; Rn.102180; -.
DR   ProteinModelPortal; P20171; -.
DR   SMR; P20171; 1-171.
DR   MINT; MINT-4996514; -.
DR   STRING; P20171; -.
DR   UCSC; BC086608; rat.
DR   RGD; 2827; Hras.
DR   eggNOG; maNOG09147; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P20171; -.
DR   PhylomeDB; P20171; -.
DR   Genevestigator; P20171; -.
DR   GermOnline; ENSRNOG00000016611; Rattus norvegicus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IMP:RGD.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:RGD.
DR   GO; GO:0035176; P:social behavior; IEP:RGD.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Complete proteome; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Palmitate; Prenylation; Proto-oncogene; S-nitrosylation.
FT   CHAIN         1    186       GTPase HRas.
FT                                /FTId=PRO_0000043000.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    186       GTPase HRas, N-terminally processed.
FT                                /FTId=PRO_0000326479.
FT   PROPEP      187    189       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000043001.
FT   NP_BIND      10     17       GTP.
FT   NP_BIND      57     61       GTP.
FT   NP_BIND     116    119       GTP.
FT   REGION      166    185       Hypervariable region.
FT   MOTIF        32     40       Effector region.
FT   MOD_RES       1      1       N-acetylmethionine; in GTPase HRas;
FT                                alternate (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine; in GTPase HRas, N-
FT                                terminally processed (By similarity).
FT   MOD_RES     118    118       S-nitrosocysteine (By similarity).
FT   MOD_RES     186    186       Cysteine methyl ester.
FT   LIPID       181    181       S-palmitoyl cysteine (By similarity).
FT   LIPID       184    184       S-palmitoyl cysteine.
FT   LIPID       186    186       S-farnesyl cysteine.
FT   MUTAGEN      26     26       N->G: Interacts and partially stimulates
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      35     35       T->S: No interaction and stimulation of
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      37     37       E->G: Reduced interaction and stimulation
FT                                of PLCE1; when associated with L-61.
FT   MUTAGEN      38     38       D->N: Reduced interaction and stimulation
FT                                of PLCE1; when associated with L-61.
FT   MUTAGEN      40     40       Y->C: No interaction and stimulation of
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      61     61       Q->L: Constitutively active.
FT                                Constitutively interacts and stimulates
FT                                PLCE1 phospholipase activity. Reduced
FT                                interaction and stimulation of PLCE1;
FT                                when associated with G-37 and N-38. No
FT                                interaction and stimulation of PLCE1;
FT                                when associated with S-35 and C-40.
FT                                Interacts and partially stimulates PLCE1;
FT                                when associated with G-26. Interacts but
FT                                does not stimulate PLCE1; when associated
FT                                with S-186.
FT   MUTAGEN     186    186       C->S: Interacts but does not stimulate
FT                                PLCE1; when associated with L-61.
SQ   SEQUENCE   189 AA;  21314 MW;  EE6DD9B533E2856A CRC64;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGLG
     CMSCKCVLS
//